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  • View Data Sheet

    Description:

    Bone Morphogenetic Protein-7 Human Recombinant, His Tag

    Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.

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    CYT-629

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    • sds-page

    Description

    BMP7 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 148 amino acids (293-431) and having a molecular mass of 16.8 kDa. The BMP-7 is fused to 8 amino acid His Tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-7 protein (0.5mg/ml) solution contains 10mM sodium citrate pH3.5 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    More Info

    • Introduction

      The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.

    • Synonyms

      Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.

    • Background

      Research Paper on Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer, HEK

      Abstract:

      Step into the fascinating world of Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer (BMP-7 HR) in Human Embryonic Kidney Cells (HEK). In this research paper, we embark on an exciting journey to uncover the wonders of BMP-7 HR and its significance in cellular differentiation. As a pivotal member of the transforming growth factor-beta (TGF-β) superfamily, BMP-7 HR holds immense potential in tissue regeneration and development. Join us as we delve into the intricate molecular mechanisms of BMP-7 HR signaling in HEK cells while also exploring its friendly interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).

      Introduction:

      Welcome to the world of BMP-7 HR! In this section, we introduce the remarkable BMP-7 HR and its essential role in guiding cellular differentiation. Let's get to know our loyal companion, Human Embryonic Kidney Cells (HEK), as they help us unveil the secrets of BMP-7 HR signaling.

      BMP-7 HR Signaling in HEK Cells:

      Be amazed by the graceful dance of BMP-7 HR signaling within HEK cells! Uncover the captivating process of ligands binding to specific receptors, setting the stage for both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay orchestrates various cellular processes, including gene transcription, cell proliferation, and differentiation.

      Influential Role in Cellular Differentiation:

      Watch in awe as BMP-7 HR takes center stage as a master conductor of cellular differentiation within HEK cells. Marvel at its ability to promote osteogenic differentiation, leading to the expression of vital osteogenic markers like RUNX2 and Osteocalcin. But that's not all! Join us in exploring BMP-7 HR's versatile nature, influencing other forms of differentiation, such as chondrogenic and adipogenic pathways.

      Interplay with Key Cytokines:

      Uncover the intriguing interactions between BMP-7 HR and key cytokines like TNF-α and TNFSF2. Witness how BMP-7 HR modulates the expression and activity of these cytokines, hinting at potential cross-talk between BMP-7 HR and inflammatory pathways, fostering a harmonious cellular environment.

      Therapeutic Implications and Tissue Regeneration:

      The therapeutic potential of BMP-7 HR in tissue regeneration comes to the forefront. Together, we explore the exciting possibilities of utilizing BMP-7 HR in regenerative medicine, offering hope for healing and tissue repair. As we navigate this path, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring the best outcomes.

      Conclusion:

      As we conclude our exploration of BMP-7 HR in HEK cells, we stand in awe of its role in guiding cellular differentiation and tissue regeneration. Equipped with this knowledge, we look forward to a future where BMP-7 HR opens doors to innovative applications in regenerative medicine, making a positive impact on human health and well-being.

      What is the molecular weight/Mw of BMP7 Protein?
      BMP7 Protein has a total Mw of 16.8kDa.

      What is the source or expression system of BMP7 Protein?
      Escherichia Coli.

      What is the Purity of BMP7 Protein?
      BMP7 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP7 Protein?
      The biological functionality of BMP7 Protein will be determined in the future.

      What is the amino acid sequence of BMP7 Protein?
      MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.

      What applications can BMP7 Protein be used in?
      BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP7 Protein?
      The endotoxin level is minimal, BMP7 Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Bmp 7 Human His
  • View Data Sheet

    Description:

    Otoraplin Human Recombinant

    Otoraplin, Fibrocyte-derived protein, Melanoma inhibitory activity-like protein, OTOR, MIAL, FDP, MIAL1, MGC126737, MGC126739.

    Product # :

    CYT-582

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    Description

    Otoraplin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12.7 kDa.The OTOR is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The OTOR protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 130mM NaCl.

    Purity

    Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      OTOR proteins is also known as fibrocyte-derived protein (Fdp) and Melanoma inhibitory activity-like (MIAL). Otoraplin is a member of the melanoma-inhibiting activity gene family. Otoraplin is a secreted 16 kDa globular protein that is expressed in the inner ear by periotic mesenchyme and developing and mature fibrocytes. OTOR is highly homologous to MIA/cartilage-derived retinoic acid-sensitive protein (CD-RAP), which is a cartilage-specific protein that is also expressed in malignant melanoma cells. The 111 amino acid mature human otoraplin contains 1 SH3 domain (46 – 107 amino acids) and a Tyr at position 50 that is reportedly sulfated. Otoraplin takes pasrt in the initiation of periotic mesenchyme chondrogenesis.
      Otoraplin is secreted through the Golgi apparatus and plays a role in cartilage development and maintenance. A frequent polymorphism in the translation start codon of OTOR can abolish translation and may be associated with forms of deafness.

    • Synonyms

      Otoraplin, Fibrocyte-derived protein, Melanoma inhibitory activity-like protein, OTOR, MIAL, FDP, MIAL1, MGC126737, MGC126739.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized OTOR Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OTOR should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Otoraplin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VHGIFMDRLASKKLCADDECVYTISLASAQEDYNAPDCRFINVKKGQQIYVYS
      KLVKENGAGEFWAGSVYGDGQDEMGVVGYFPRNLVKEQRVYQEATKEVPTT
      DIDFFCE.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Otoraplin Human
  • View Data Sheet

    Description:

    Bone Morphogenetic Protein Receptor Type IA Human Recombinant

    BMPR-1A, BMP-R1A, BMPR1A, BMR1A, CD292, CD-292, Serine/threonine-protein kinase receptor R5, SKR5, ALK-3, ACVRLK3, EC 2.7.11.30, CD292 antigen.

    Product # :

    CYT-380

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    Description

    BMPR1A Human Recombinant extracellular domain produced in baculovirus is a monomeric, glycosylated, Polypeptide chain fused with 6xHis tag at C-terminus and having a molecular mass of 23 kDa. The BMR1A is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    CD292 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1X PBS.

    Purity

    Greater than 90.0% as determined by
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Measured by its ability to inhibit recombinant human BMP-2 induced alkaline phosphatase production by C2C12 myogenic cells. The ED50 for this effect is typically 1-3 µg/ml in the presence of 500 ng/ml of recombinant human BMP-2 corresponding to a Specific Activity of 2,000 units/mg.

    More Info

    • Introduction

      The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF-beta superfamily. TGF-betas transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding.

    • Synonyms

      BMPR-1A, BMP-R1A, BMPR1A, BMR1A, CD292, CD-292, Serine/threonine-protein kinase receptor R5, SKR5, ALK-3, ACVRLK3, EC 2.7.11.30, CD292 antigen.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bone Morphogenetic Protein Receptor 1A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMPR1A should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized ALK-3 in sterile PBS not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      Bone Morphogenetic Protein Receptor Type IA Human Recombinant: Exploring the Potential of a Key Regulator in Bone Development

      Abstract:

      Bone Morphogenetic Protein Receptor Type IA (BMPR1A) human recombinant is a crucial regulator in bone development and homeostasis. This research paper provides a comprehensive analysis of BMPR1A, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMPR1A human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.

      Introduction:

      Bone development and maintenance rely on intricate signaling pathways, with BMPR1A playing a pivotal role in bone morphogenesis. This paper explores the unique features of BMPR1A and presents novel approaches for its production and optimization, aiming to uncover its therapeutic potential in bone-related disorders.

      Characteristics and Signaling Pathways:

      BMPR1A belongs to the serine/threonine kinase receptor family and is expressed predominantly in skeletal tissues. It binds bone morphogenetic proteins (BMPs), initiating intracellular signaling cascades that regulate osteoblast differentiation and bone formation. BMPR1A activates the Smad-dependent and Smad-independent pathways, leading to the activation of transcription factors involved in bone-specific gene expression.

      Production of BMPR1A Human Recombinant:

      Efficient production methodologies are critical for harnessing the therapeutic potential of BMPR1A human recombinant. Mammalian cell-based expression systems, such as Chinese hamster ovary (CHO) cells, have been utilized to ensure proper folding and post-translational modifications. Optimization strategies, including codon optimization and vector engineering, have been employed to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to obtain high-quality BMPR1A recombinant protein.

      Potential Therapeutic Applications:

      BMPR1A human recombinant holds significant promise in regenerative medicine. Disruption of BMP signaling has been implicated in skeletal disorders, including bone fractures, osteoporosis, and skeletal dysplasias. Modulating BMPR1A activity using BMPR1A human recombinant may provide a targeted therapeutic approach for promoting bone regeneration, fracture healing, and bone tissue engineering. Furthermore, BMPR1A signaling plays a role in other tissues, such as the cardiovascular system and nervous system, suggesting broader therapeutic applications.

      Conclusion:

      BMPR1A human recombinant represents a crucial regulator in bone development and holds immense potential in regenerative medicine. Optimizing production methodologies and further understanding its signaling pathways will enhance its clinical utility. With its implications in skeletal disorders and potential applications in other tissues, BMPR1A human recombinant stands as a promising tool for promoting bone regeneration and tissue engineering.

      What is the molecular weight/Mw of BMPR1A Protein?
      BMPR1A Protein has a total Mw of 23kDa.

      What is the source or expression system of BMPR1A Protein?
      Insect Cells.

      What is the Purity of BMPR1A Protein?
      BMPR1A Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMPR1A Protein?
      Measured by its ability to inhibit recombinant human BMP-2 induced alkaline phosphatase production by C2C12 myogenic cells. The ED50 for this effect is typically 1-3 µg/ml in the presence of 500 ng/ml of recombinant human BMP-2 corresponding to a Specific Activity of 2,000 units/mg.

      What applications can BMPR1A Protein be used in?
      BMPR1A Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMPR1A Protein?
      The endotoxin level is minimal, BMPR1A Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Bmpr1A Human
  • View Data Sheet

    Description:

    Syntaxin-1A Human Recombinant

    STX1, HPC-1, p35-1, Syntaxin-1A, Neuron-specific antigen HPC-1, STX-1A, STX1A.

    Product # :

    PRO-574

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    Description

    Syntaxin-1A Human Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids (1-226) and having a molecular mass of 26.1 kDa.Recombinant Human STX1A contains N-terminal domain (Habc) and t_SNARE domain (H3 domain).

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris-HCl pH7.5, 10% glycerol, and 1mM DTT.

    Purity

    Greater than 95.0% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      Syntaxin is membrane integrated Q-SNARE protein participating in exocytosis. Syntaxin is composed of an N-terminal regulatory domain (Habc), a SNARE domain (known as H3), and a single C-terminal transmembrane domain. The SNARE (H3) domain binds to both synaptobrevin and SNAP-25 forming the core SNARE complex. Synaptic vesicles store neurotransmitters that are released during calcium-regulated exocytosis. The specificity of neurotransmitter release requires the localization of both synaptic vesicles and calcium channels to the presynaptic active zone. Syntaxins function in this vesicle fusion process. Syntaxins also serve as a substrate for botulinum neurotoxin type C, a metalloprotease that blocks exocytosis and has high affinity for a molecular complex that includes the alpha-latrotoxin receptor which produces exocytosis.

    • Synonyms

      STX1, HPC-1, p35-1, Syntaxin-1A, Neuron-specific antigen HPC-1, STX-1A, STX1A.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MKDRTQELRT AKDSDDDDDV AVTVDRDRFM DEFFEQVEEI RGFIDKIAEN VEEVKRKHSA ILASPNPDEK TKEELEELMS DIKKTANKVR SKLKSIEQSI EQEEGLNRSS ADLRIRKTQH STLSRKFVEV MSEYNATQSD YRERCKGRIQ RQLEITGRTT TSEELEDMLE SGNPAIFASG IIMDSSISKQ ALSEIETRHS EIIKLENSIR ELHDMFMDMA MLVESQ.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Stx1A Human
  • View Data Sheet

    Description:

    ER Lipid Raft Associated 2 Protein Human Recombinant

    Erlin-2, Endoplasmic reticulum lipid raft-associated protein 2, Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 2, SPFH domain-containing protein 2,ERLIN2, C8orf2, SPFH2, UNQ2441, PRO5003, PRO9924, NET32, SPG18.

    Product # :

    PRO-1266

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    Description

    ERLIN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 338 amino acids (25-339 a.a) and having a molecular mass of 37.8 kDa.ERLIN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ERLIN2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      ER Lipid Raft Associated 2 (ERLIN2) is a domain-containing protein which is a member of the band 7/mec-2 family. ERLIN2 is a ubiquitously expressed 339 amino acid protein.ERLIN2 which is localized to the lipid raft-like domains in the membrane of the endoplasmic reticulum (ER), plays a key role in the ER-associated degradation (ERAD) pathway that eliminates metabolically regulated and abnormal proteins from the ER.

    • Synonyms

      Erlin-2, Endoplasmic reticulum lipid raft-associated protein 2, Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 2, SPFH domain-containing protein 2,ERLIN2, C8orf2, SPFH2, UNQ2441, PRO5003, PRO9924, NET32, SPG18.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSKIEEGHI GVYYRGGALL TSTSGPGFHL MLPFITSYKS VQTTLQTDEV KNVPCGTSGG VMIYFDRIEV VNFLVPNAVY DIVKNYTADY DKALIFNKIH HELNQFCSVH TLQEVYIELF DQIDENLKLA LQQDLTSMAP GLVIQAVRVT KPNIPEAIRR NYELMESEKT KLLIAAQKQK VVEKEAETER KKALIEAEKV AQVAEITYGQ KVMEKETEKK ISEIEDAAFL AREKAKADAE CYTAMKIAEA NKLKLTPEYL QLMKYKAIAS NSKIYFGKDI PNMFMDSAGS VSKQFEGLAD KLSFGLEDEP LETATKEN.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Erlin2 Human
  • View Data Sheet

    Description:

    Syntaxin-3 Human Recombinant

    Syntaxin-3, STX3, STX3A.

    Product # :

    PRO-1082

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    Description

    STX3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids (1-263 a.a) and having a molecular mass of 33.2kDa.STX3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    STX3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Syntaxin 3 (STX3) is a member of the syntaxin family. The syntaxin family members are cellular receptors for transport vesicles which participate in exocytosis in neutrophils. STX3 has a significant role in the growth of neurites and functions as a direct target for omega-6 arachidonic acid. STX3 is steered to the apical membrane of epithelial cells where it forms clusters and is vital in establishing and maintaining polarity required for protein trafficking involving vesicle fusion and exocytosis.

    • Synonyms

      Syntaxin-3, STX3, STX3A.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMMKDRL EQLKAKQLTQ DDDTDAVEIA IDNTAFMDEF FSEIEETRLN IDKISEHVEE AKKLYSIILS APIPEPKTKD DLEQLTTEIK KRANNVRNKL KSMEKHIEED EVRSSADLRI RKSQHSVLSR KFVEVMTKYN EAQVDFRERS KGRIQRQLEI TGKKTTDEEL EEMLESGNPA IFTSGIIDSQ ISKQALSEIE GRHKDIVRLE SSIKELHDMF MDIAMLVENQ GEMLDNIELN VMHTVDHVEK ARDETKKAVK YQSQARKK.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Stx3 Human
  • View Data Sheet

    Description:

    Fibroblast Growth Factor-18 Mouse Recombinant

    Fibroblast growth factor 18, FGF-18, zFGF5, Fgf18, D130055P09Rik.

    Product # :

    CYT-064

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    • sds-page

    Description

    FGF-18 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 180 amino acids and having a molecular mass of 21kDa.The FGF-18 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FGF-18 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.

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    • Introduction

      Fibroblast growth factor 18 (FGF18) is a member of the large FGF family which has at least 23 members. FGF18 is a heparin binding growth factor with a core 120 amino acid FGF domain which allows for a common tertiary structure. FGFs are expressed in the course of the embryonic development and in restricted adult tissues. FGF-18 is an indispensable regulator of long bone and calvarial development. FGF-18 signals via FGFR 1c, 2c, 3c, and 4.

    • Synonyms

      Fibroblast growth factor 18, FGF-18, zFGF5, Fgf18, D130055P09Rik.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF-18 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-18 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized FGF-18 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQAELQK PFKYTTVTKR SRRIRPTHPG.

    • Background

      What is the molecular weight/Mw of FGF18 Protein?
      FGF18 Protein has a total Mw of 21kDa.

      What is the source or expression system of FGF18 Protein?
      Escherichia Coli.

      What is the Purity of FGF18 Protein?
      FGF18 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF18 Protein?
      The ED50 as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.

      What is the amino acid sequence of FGF18 Protein?
      EENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQAELQK PFKYTTVTKR SRRIRPTHPG.

      What applications can FGF18 Protein be used in?
      FGF18 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF18 Protein?
      The endotoxin level is minimal, FGF18 Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Fgf 18 Mouse
  • View Data Sheet

    Description:

    Fibroblast Growth Factor-basic Human Recombinant, Thermostable

    HBGH-2, HBGF-2, FGF-2, FGF-b, HBGH2, HBGF2, FGF2, FGFb, FGF2 Thermostable, FGF-2 Thermostable.

    Product # :

    CYT-943

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    Description

    FGF2 Thermostable is a stabilized form of FGF2 growth factor which enables a novel method to produce FGF2-dependent cell cultures more efficiently, having less media changes. FGF2 Thermostable can maintain its biological activity even after five days at 37°C. The increase in the stability of FGF2 in cell-culture enables a more homogenous, undifferentiated stem cell culture, while saving scientists crucial time and money, as frequent supplementation of FGF-basic and the everyday medium change is not necessary. Thermostable FGF-2 is a hyperstable protein. The Thermal stability of the protein is increased by 15°C compared to the wild-type FGF-2. Thermostable FGF-2 is more than 5-times prolonged half-life in human cell culture incubated at 37°C. The FGF-2 Thermostable protein is engineered with fully retained biological function and has no harmful stabilizing additives.Thermostable FGF2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids and having a total calculated molecular mass is 17.2kDa.

    Source

    Escherichia Coli.

    Formulation

    FGF Basic Thermostable was lyophilized from 20mM Tris-HCl, 150mM NaCl & 5% Trehalose, pH-7.6.

    Purity

    Purity is greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as calculated by the dose-dependent proliferation of murine balb/c 3T3 cells is less than 0.05ng/ml, corresponding to a specific activity of >20,000,000 units/mg

    More Info

    • Synonyms

      FGF2 Thermostable, FGF-basic Thermostable.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Thermostable FGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF2 Thermostable should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized FGF2 thermostable protein in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AAGSITTLPA LPEDGGSGAF PPGHFKDPKL LYCKNGGFFL RIHPDGRVDG TRDKSDPFIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL YAIKNVTDEC FFFERLEENN YNTYRSRKYP SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS

    • Background

      Why Choose FGF2 Thermostable?
      FGF2 can lose much of its activity after 1-2 days at 37°C due to unfolding and degradation. Thermostable FGF2 is engineered with amino acid substitutions that increase structural stability without significantly altering receptor binding or biological function.

      What are the advantages of FGF2 Protein?
      *Better maintenance of pluripotency markers
      *Higher colony quality
      *Faster expansion rates
      *Reduced spontaneous differentiation
      *Greater viability after passaging

      What is the source or expression system of FGF2 Protein?
      Escherichia Coli.

      What is the Purity of FGF2 Protein?
      FGF2 Protein is >95% pure as determined by SDS-PAGE.

      What is the molecular weight / Mw of FGF2 Protein?
      FGF2 Protein having a total Mw of 17.2kDa.

      What is the Biological Activity of FGF2 Protein?
      The ED50 as calculated by the dose-dependent proliferation of murine balb/c 3T3 cells is less than 0.05ng/ml, corresponding to a specific activity of >20,000,000 units/mg.

      What is the endotoxin level for FGF2 Protein?
      The endotoxin level is minimal, FGF2 Protein was purified using conventional chromatography techniques.

      What is the amino acid sequence of FGF2 Protein?
      AAGSITTLPA LPEDGGSGAF PPGHFKDPKL LYCKNGGFFL RIHPDGRVDG TRDKSDPFIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL YAIKNVTDEC FFFERLEENN YNTYRSRKYP SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS

      Is FGF2 Protein conjugated to a Tag?
      FGF2 Protein is not conjugated to a tag.

      What applications can FGF2 Protein be used in?
      FGF2 Protein can probably be used in western blot, ELISA and Lateral Flow.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Fgf2 Human Thermostable
  • View Data Sheet

    Description:

    Thymus Expressed Chemokine Human Recombinant (CCL25)

    C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.

    Product # :

    CHM-364

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    Description

    TECK Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 14.2kDa. The TECK is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 150mM NaCl.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract human monocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    More Info

    • Introduction

      CCL25 (Teck) is a novel CC chemokine, which is distantly related (about 20% amino acid sequence identity) to other CC chemokines. The mouse CCL25 cDNA has also been cloned and shown to encode a 144 a.a. protein, which exhibits 49% a.a. sequence identity to the human CCL25. Human and mouse CCL25 expression was shown to be greatly restricted to the thymus and small intestine. While dendritic cells are identified as the source of CCL25 production in the thymus, dendritic cells derived from bone marrow do not express CCL25. CCL25 signals through the CCR9 receptor. Teck is possibly involved in T-cell development.
      Recombinant human and mouse Teck were shown to be chemotactic for activated macrophages, dendritic cells and thymocytes. The recombinant protein demonstrates chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritic cells but is inactive on peripheral blood lymphocytes and neutrophils.

    • Synonyms

      C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TECK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TECK should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized TECK in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QGVFEDCCLA YHYPIGWAVL RRAWTYRIQE VSGSCNLPAA IFYLPKRHRK VCGNPKSREV QRAMKLLDAR NKVFAKLHHN MQTFQAGPHA VKKLSSGNSK LSSSKFSNPI SSSRKNVSLL ISANSGL.

    • Background

      What is the molecular weight/Mw of CCL25 HUMAN Protein?
      CCL25 HUMAN Protein has a total Mw of 14.2kDa.

      What is the source or expression system of CCL25 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL25 HUMAN Protein?
      CCL25 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL25 HUMAN Protein?
      Determined by its ability to chemoattract human monocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

      What is the amino acid sequence of CCL25 HUMAN Protein?
      QGVFEDCCLA YHYPIGWAVL RRAWTYRIQE VSGSCNLPAA IFYLPKRHRK VCGNPKSREV QRAMKLLDAR NKVFAKLHHN MQTFQAGPHA VKKLSSGNSK LSSSKFSNPI SSSRKNVSLL ISANSGL.

      What applications can CCL25 HUMAN Protein be used in?
      CCL25 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL25 HUMAN Protein?
      The endotoxin level is minimal, CCL25 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL25 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CCL25 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Teck Human
  • View Data Sheet

    Description:

    Vascular Endothelial Growth Factor Receptor-1 D1-7 Mouse Recombinant

    FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    Product # :

    PKA-312

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    Description

    Soluble FLT1 Mouse Recombinant fused with the Fc part of human IgG1 produced in baculovirus is disulfide-linked homodimeric , polypeptide containing 965 amino acids. The monomers have a molecular mass of 130 kDa. The soluble receptor protein contains all 7 extracellular domains (Tyr23-Asn757), which contain all the information necessary for high affinity ligand binding.

    Source

    Insect Cells.

    Formulation

    FLT1 D1-7 was lyophilized from a concentrated (1 mg/ml) sterile solution containing PBS Buffer.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity of sVEGFR-1/Fc was determined by its ability to inhibit the VEGF-dependent proliferation of human umbilical vein endothelial cells.

    More Info

    • Introduction

      Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

    • Synonyms

      FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FLT-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution FLT1 should be stored at 4C between 2-7 days and for future use below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized FLT1 Fc/Chimera in PBS not less than 50µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      YGSGSKLKVP ELSLKGTQHV MQAGQTLFLK CRGEAAHSWS LPTTVSQEDK RLSITPPSAC GRDNRQFCST LTLDTAQANH TGLYTCRYLP TSTSKKKKAE SSIYIFVSDA GSPFIEMHTD IPKLVHMTEG RQLIIPCRVT SPNVTVTLKK FPFDTLTPDG QRITWDSRRG FIIANATYKE IGLLNCEATV NGHLYQTNYL THRQTNTILD VQIRPPSPVR LLHGQTLVLN CTATTELNTR VQMSWNYPGK ATKRASIRQR IDRSHSHNNV FHSVLKINNV ESRDKGLYTC RVKSGSSFQS FNTSVHVYEK GFISVKHRKQ PVQETTAGRR SYRLSMKVKA FPSPEIVWLK DGSPATLKSA RYLVHGYSLI IKDVTTEDAG DYTILLGIKQ SRLFKNLTAT LIVNVKPQIY EKSVSSLPSP PLYPLGSRQV LTCTVYGIPR PTITWLWHPC HHNHSKERYD FCTENEESFI LDPSSNLGNR IESISQRMTV IEGTNKTVST LVVADSQTPG IYSCRAFNKI GTVERNIKFY VTDVPNGFHV SLEKMPAEGE DLKLSCVVNK FLYRDITWIL LRTVNNRTMH HSISKQKMAT TQDYSITLNL VIKNVSLEDS GTYACRARNI YTGEDILRKT EVLVRDSEAP HLLQNLSDYE VSISGSTTLD CQARGVPAPQ ITWFKNNHKI QQEPGIILGP GNSTLFIERV TEEDEGVYRC RATNQKGAVE SAAYLTVQGT SDKSNAASDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSREEMTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPMLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGK

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Flt1 D7 Mouse
  • View Data Sheet

    Description:

    Galactokinase 1 Human Recombinant

    Galactose kinase, GK1, GALK, EC 2.7.1.6, GALK1.

    Product # :

    PKA-264

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    Description

    GALK1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 412 amino acids (1-392 a.a.) and having a molecular mass of 44.4 kDa. The GALK1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GALK1 Human (0.5mg/ml) solution containing 20% glycerol 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GALK1 enzyme is needed in the first step of the galactose metabolism pathway.
      (ATP + D-galactose = ADP + alpha-D-galactose 1-phosphate). GALK1 deficinecy lead galactosemia II which is an autosomal recessive deficiency known by congenital cataracts during infancy and presenile cataracts in the adult population. The cataracts are secondary to accumulation of galactitol in the lenses.

    • Synonyms

      Galactose kinase, GK1, GALK, EC 2.7.1.6, GALK1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAALRQPQVA ELLAEARRAF REEFGAEPEL AVSAPGRVNL IGEHTDYNQG LVLPMALELM TVLVGSPRKD GLVSLLTTSE GADEPQRLQF PLPTAQRSLE PGTPRWANYV KGVIQYYPAA PLPGFSAVVV SSVPLGGGLS SSASLEVATY TFLQQLCPDS GTIAARAQVC QQAEHSFAGM PCGIMDQFIS LMGQKGHALL IDCRSLETSL VPLSDPKLAV LITNSNVRHS LASSEYPVRR RQCEEVARAL GKESLREVQL EELEAARDLV SKEGFRRARH VVGEIRRTAQ AAAALRRGDY RAFGRLMVES HRSLRDDYEV SCPELDQLVE AALAVPGVYG SRMTGGGFGG CTVTLLEASA APHAMRHIQE HYGGTATFYL SQAADGAKVL CL.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Galk1 Human
  • View Data Sheet

    Description:

    Kallikrein-7 Human Recombinant

    kallikrein-related peptidase 7, SCCE, hSCCE, EC 3.4.21.117, hK7, Kallikrein-7, PRSS6, KLK7.

    Product # :

    ENZ-510

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    Description

    KLK7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 249 amino acids (30-253) and having a molecular mass of 27.1 kDa.The KLK7 is fused to a 25 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KLK7 protein 1mg/ml is supplied in 20mM Tris-HCl, pH-8, 2M Urea and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      KLK7 catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. KLK7 is involved in the activation of precursors to inflammatory cytokines.

    • Synonyms

      kallikrein-related peptidase 7, SCCE, hSCCE, EC 3.4.21.117, hK7, Kallikrein-7, PRSS6, KLK7.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMIIDGA PCARGSHPWQ VALLSGNQLH CGGVLVNERW VLTAAHCKMN EYTVHLGSDT LGDRRAQRIK ASKSFRHPGY STQTHVNDLM LVKLNSQARL SSMVKKVRLP SRCEPPGTTC TVSGWGTTTS PDVTFPSDLM CVDVKLISPQ DCTKVYKDLL ENSMLCAGIP DSKKNACNGD SGGPLVCRGT LQGLVSWGTF PCGQPNDPGV YTQVCKFTKW INDTMKKHR.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Klk7 Human
  • View Data Sheet

    Description:

    Kirsten Rat Sarcoma Viral Oncogene, Isoform 2B Human Recombinant

    C-K-RAS, K-RAS2A, K-RAS2B, K-RAS4A, K-RAS4B, KI-RAS, KRAS1, NS3, RASK2, c-Ki-ras, GTPase KRas, Kirsten Rat Sarcoma Viral Oncogene, KRAS.

    Product # :

    PRO-854

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    Description

    KRAS 2B Recombinant human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 205 amino acids (1-185 a.a.) and having a molecular mass of 23.2 kDa. The Human KRAS 2B is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KRAS 2B Human solution containing 20mM Tris-HCl pH-8, 0.1M NaCl, 1mM DTT & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      KRAS is part of the small GTPase superfamily. A single amino acid substitution is accountable for an activating mutation. KRAS participates in various malignancies, including lung adenocarcinoma, mucinous adenoma, ductal carcinoma of the pancreas and colorectal carcinoma.

    • Synonyms

      C-K-RAS, K-RAS2A, K-RAS2B, K-RAS4A, K-RAS4B, KI-RAS, KRAS1, NS3, RASK2, c-Ki-ras, GTPase KRas, Kirsten Rat Sarcoma Viral Oncogene, KRAS.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG HEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHHYREQI KRVKDSEDVP MVLVGNKCDL PSRTVDTKQA QDLARSYGIP FIETSAKTRQ GVDDAFYTLV REIRKHKEKM SKDGKKKKKK SKTKC.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Kras Human
  • View Data Sheet

    Description:

    Latexin Human Recombinant

    LXN, TCI, ECI, Latexin, Endogenous carboxypeptidase inhibitor, Tissue carboxypeptidase inhibitor, MUM.

    Product # :

    ENZ-407

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    Description

    Recombinant Human Latexin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids and having a molecular mass of 25.7kDa. Latexin is purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The Latexin protein solution contains 20mM Tris-HCl, pH-7.5, 50mM NaCl and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Latexin enzyme is a carboxypeptidase A inhibitor that is highly expressed in the heart, prostate, ovary, kidney, pancrease, brain and colon. Latexin has no noticeable sequence resemblance with plant and parasite inhibitors, however it is related to a human putative tumor suppressor protein, TIG1. Latexin is down-regulated in the presenilin-1-deficient mouse brain, thus putatively playing a role in Alzheimer's disease.

    • Synonyms

      LXN, TCI, ECI, Latexin, Endogenous carboxypeptidase inhibitor, Tissue carboxypeptidase inhibitor, MUM.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MEIPPTNYPA SRAALVAQNY INYQQGTPHR VFEVQKVKQA SMEDIPGRGH KYRLKFAVEE IIQKQVKVNC TAEVLYPSTG QETAPEVNFTFEGETGKNPD EEDNTFYQRL KSMKEPLEAQ NIPDNFGNVS PEMTLVLHLA WVACGYIIWQ NSTEDTWYKM VKIQTVKQVQ RNDDFIELDYTILLHNIASQ EIIPWQMQVL WHPQYGTKVK HNSRLPKEVQ LE.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Latexin Human
  • View Data Sheet

    Description:

    Centrin-3 Human Recombinant

    CEN3, CEN-3, CETN-3.

    Product # :

    PRO-533

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    Description

    CETN3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 187 amino acids (1-167 a.a.) and having a molecular mass of 21.7 kDa. CETN3 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    CETN3 Human 0.5mg/ml solution contains 20mM Trsi HCl pH-8, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      CETN3 comprises of 4 EF-hand calcium binding domains, and is a part of the centrin protein family. CETN3 protein is widely expressed cytoskeletal components that demonstrate increased expression during cell differentiation. CETN3 takes part in centrosome reproduction.

    • Synonyms

      CEN3, CEN-3, CETN-3.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSLALRSELV VDKTKRKKRR ELSEEQKQEI KDAFELFDTD KDEAIDYHEL KVAMRALGFD VKKADVLKIL
      KDYDREATGK ITFEDFNEVV TDWILERDPH EEILKAFKLF DDDDSGKISL RNLRRVAREL GENMSDEELR AMIEEFDKDG DGEINQEEFI
      AIMTGDI.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Cetn3 Human
  • View Data Sheet

    Description:

    GRO-Gamma Rat Recombinant (CXCL3), CINC-2 alpha

    Cytokine-induced neutrophil chemoattractant 2, CINC2, CINC-2, Macrophage inflammatory protein 2-alpha.

    Product # :

    CHM-258

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    Description

    GRO-g Rat Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7.8kDa. The CXCL3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Rat CXCL3 lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract 293 transfected CXCR2 cells using a concentration range of 10-100 ng/ml, corresponding to a specific activity of 10,000-100,000 units/mg.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.

    • Synonyms

      Cytokine-induced neutrophil chemoattractant 2, CINC2, CINC-2, Macrophage inflammatory protein 2-alpha.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GRO-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized GRO-gamma in sterile 18Mcm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      RELRCQCLKT LPRVDFENIQ SLTVTPPGPH CTQTEVIATL KDGQEVCLNP QAPRLQKIIQ KLLKSDKSS.

    • Background

      What is the molecular weight/Mw of CXCL3 RAT ALPHA Protein?
      CXCL3 RAT ALPHA Protein has a total Mw of 7.8kDa.

      What is the source or expression system of CXCL3 RAT ALPHA Protein?
      Escherichia Coli.

      What is the Purity of CXCL3 RAT ALPHA Protein?
      CXCL3 RAT ALPHA Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL3 RAT ALPHA Protein?
      Determined by its ability to chemoattract 293 transfected CXCR2 cells using a concentration range of 10-100 ng/ml, corresponding to a specific activity of 10,000-100,000 units/mg.

      What is the amino acid sequence of CXCL3 RAT ALPHA Protein?
      RELRCQCLKT LPRVDFENIQ SLTVTPPGPH CTQTEVIATL KDGQEVCLNP QAPRLQKIIQ KLLKSDKSS.

      What applications can CXCL3 RAT ALPHA Protein be used in?
      CXCL3 RAT ALPHA Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL3 RAT ALPHA Protein?
      The endotoxin level is minimal, CXCL3 RAT ALPHA Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL3 RAT ALPHA that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL3 RAT ALPHA?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Gro G Rat Cinc 2A
  • View Data Sheet

    Description:

    RAB31, Member RAS Oncogene Family Recombinant Human

    Ras-related protein Rab-31, Ras-related protein Rab-22B, RAB31, RAB22B.

    Product # :

    PRO-1090

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    Description

    RAB31 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-195 a.a) and having a molecular mass of 25.9kDa.RAB31 is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RAB31 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 30% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      RAB31 Member RAS Oncogene Family (RAB31) is a 194 amino lipid-anchored protein which localizes to the cytoplasmic side of the cell membrane and is a member of the Ras related GTPase superfamily. RAB31 is expressed at high levels in the lung, brain and heart. RAB31 functions in a similar mode to other Rab proteins, namely playing a part in protein transport. Small GTP-binding proteins of the RAB family, for example RAB31, play critical roles in vesicle and granule targeting. RAB31 gas the highest expression in the placenta and brain with lower levels in the heart and lung. However, RAB31 is not detected in liver, skeletal muscle, kidney or pancreas.

    • Synonyms

      Ras-related protein Rab-31, Ras-related protein Rab-22B, RAB31, RAB22B.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMMA IRELKVCLLG DTGVGKSSIV CRFVQDHFDH NISPTIGASF MTKTVPCGNE LHKFLIWDTA GQERFHSLAP MYYRGSAAAV IVYDITKQDS FYTLKKWVKE LKEHGPENIV MAIAGNKCDL SDIREVPLKD AKEYAESIGA IVVETSAKNA INIEELFQGI SRQIPPLDPH ENGNNGTIKV EKPTMQASRR CC.

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    Rab31 Human
  • View Data Sheet

    Description:

    RAB32, Member RAS Oncogene Family Human Recombinant

    RAB32 member RAS oncogene family, ras-related protein Rab-32.

    Product # :

    PRO-950

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    Description

    RAB32 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 249 amino acids (1-225) and having a molecular mass of 27.6 kDa.RAB32 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RAB32 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 0.2M NaCl, 0.2M EDTA and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      RAB32 is a member of the small GTPase superfamily. RAB32 controls ER calcium management and disturbs the specific enhancement of calnexin on the MAM (mitochondria-associated membrane), however avoids affecting the ER distribution of protein-disulfide isomerase and mitofusin-2. Furthermore, RAB32 regulates the targeting of PKA (cAMP-dependent protein kinase) to mitochondrial and ER membranes and by inactivation or overexpression enhances the phosphorylation of Drp1 and Bad. Using a combination of its functions as a regulator of MAM properties and a PKA-anchoring protein, the activity and expression level of RAB32 define the speed of apoptosis onset.

    • Synonyms

      RAB32 member RAS oncogene family, ras-related protein Rab-32.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMAGGGA GDPGLGAAAA PAPETREHLF KVLVIGELGV GKTSIIKRYV HQLFSQHYRA TIGVDFALKV LNWDSRTLVR LQLWDIAGQE RFGNMTRVYY KEAVGAFVVF DISRSSTFEA VLKWKSDLDS KVHLPNGSPI PAVLLANKCD QNKDSSQSPS QVDQFCKEHG FAGWFETSAK DNINIEEAAR FLVEKILVNH QSFPNEENDV DKIKLDQETL RAENKSQCC

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Rab32 Human
  • View Data Sheet

    Description:

    Heart and Neural Crest Derivatives Expressed 1 Human Recombinant

    Heart- And Neural Crest Derivatives-Expressed Protein 1, Extraembryonic Tissues Heart Autonomic Nervous System And Neural Crest Derivatives-Expressed Protein 1, Class A Basic Helix-Loop-Helix Protein 27, BHLHa27, EHAND, Thing1, Hxt.

    Product # :

    PRO-1231

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    Description

    HAND1 Human Recombinant produced in E. coli is a single polypeptide chain containing 238 amino acids (1-215) and having a molecular mass of 26.0 kDa.HAND1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The HAND1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      HAND1 is a member of the basic helix-loop-helix family of transcription factors. HAND1 is one of two HAND proteins, two closely related family members that are irregularly expressed in the emerging ventricular chambers and have a key part in cardiac morphogenesis. Operating in a complementary manner, they work in the development of the right ventricle and aortic arch arteries, implicating them as mediators of congenital heart disease. Furthermore, HAND1 is obligatory for early trophoblast differentiation.

    • Synonyms

      Heart- And Neural Crest Derivatives-Expressed Protein 1, Extraembryonic Tissues Heart Autonomic Nervous System And Neural Crest Derivatives-Expressed Protein 1, Class A Basic Helix-Loop-Helix Protein 27, BHLHa27, EHAND, Thing1, Hxt.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMNLVGSY AHHHHHHHPH PAHPMLHEPF LFGPASRCHQ ERPYFQSWLL SPADAAPDFP AGGPPPAAAA AATAYGPDAR PGQSPGRLEA LGGRLGRRKG SGPKKERRRT ESINSAFAEL RECIPNVPAD TKLSKIKTLR LATSYIAYLM DVLAKDAQSG DPEAFKAELK KADGGRESKR KRELQQHEGF PPALGPVEKR IKGRTGWPQQ VWALELNQ

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Hand1 Human
  • View Data Sheet

    Description:

    RELM-Gamma Mouse Recombinant

    Resistin-like gamma, RELMgamma,RELM-γ, RELM-g. 

    Product # :

    CYT-1035

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    Description

    RELM g Mouse Recombinant produced in E.Coli is a non glycosylated, homodimeric polypeptide chain containing 2 x 89 amino acids and having a total molecular mass of 18.9kDa. The RELM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RELM-gamma is a novel member of the resistin-like molecule/found in inflammatory zone (RELM/FIZZ) family in mice and rats. Microarray and real-time RT-PCR experiments revealed a repression of RELMgamma mRNA in nasal respiratory epithelium of cigarette smoke-exposed versus untreated rats. The analysis of the physiological tissue-specific expression revealed highest expression in hematopoietic tissues, suggesting a cytokine-like role for RELM-gamma. RELM-gamma-mRNA is detectable in bone marrow, spleen, and lung as well as in peripheral blood granulocytes. Promyelocytic HL60 cells transfected with a RELM-gamma expression plasmid have an increased proliferation rate compared to mock-transfected cells and display an altered response to retinoic acid-induced granulocytic differentiation. Taken together, these data provide the first experimental evidence that RELM-gamma is a secreted molecule with a restricted expression pattern that may play a role in promyelocytic differentiation.

    • Synonyms

      Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized RELM g although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RELM g Mouse should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized RELM g in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MEGTLESIVE KKVKELLANR DDCPSTVTKT FSCTSITASG RLASCPSGMT VTGCACGYGC GSWDIRDGNT CHCQCSTMDW ATARCCQLA.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Mouse Relm Gamma
  • View Data Sheet

    Description:

    Relaxin-3 Human Recombinant

    Relaxin 3, Prorelaxin H3, RXN3, Insl7, ZINS4, H3, Relaxin 3 (H3), Relaxin-3, RLN3.

    Product # :

    PRO-2176

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    Description

    Relaxin-3 Human Recombinant produced in E.Coli is a disulfide-linked heterodimeric, non-glycosylated, polypeptide chain containing 24 amino acids for A chain and 27 amino acids for B chain and having a molecular mass of 2.5kDa for A chain and 3kDa for B chain.The Relaxin-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured by cAMP accumulation in human THP-1 cells, is less than 17.5ng/ml.

    More Info

    • Introduction

      Relaxin-3 (RLN3) belongs to the relaxin family. Relaxins are endocrine and autocrine/paracrine hormones. Relaxin, which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. Unlike human Relaxins 1 and 2, Relaxin 3 does not seem to have a role in reproduction; however it is involved in stress response in the brain stem. RLN3 is the only known ligand for the G-protein-coupled receptor GPCR135, titled RXFP3. In addition, RLN3 binds the LGR7 (RXFP1) receptor, however with lower affinity than Relaxin-2. Even though binding of RLN3 to LGR7 increases intracellular cAMP, binding to GPCR135 suppresses cAMP accumulation, indicating coupling to Gi, Go, or Gz by this receptor.

    • Synonyms

      Relaxin 3, Prorelaxin H3, RXN3, Insl7, ZINS4, H3, Relaxin 3 (H3), Relaxin-3, RLN3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized RLN3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Relaxin-3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized RLN3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      A chain: DVLAGLSSSC CKWGCSKSEI SSLC.
      B chain: RAAPYGVRLCG REFIRAVIFT CGGSRW.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Rln3 Human
  • View Data Sheet

    Description:

    Erythropoietin-alpha Human Recombinant, HEK

    Erythropoietin-Alpha, EPO-a, EPO-alpha, Epoetin, EP, MGC138142.

    Product # :

    CYT-083

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    Description

    EPO-a Human Recombinant produced in HEK cells is a glycosylated monomer, having a total molecular weight of 36kDa.The EPO-alpha is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The EPO-alpha was lyophilized from 1mg/ml in 1xPBS.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) and is typically 0.5-2.5ng/ml, corresponding to a specific activity of 400,000-2,000,000 units/mg.

    More Info

    • Introduction

      This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.

    • Synonyms

      Erythropoietin-Alpha, EPO-a, EPO-alpha, Epoetin, EP, MGC138142.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized EPO-alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EPO-alpha should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized EPO-alpha in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      What is the molecular weight/Mw of EPOETIN Protein?
      EPOETIN Protein has a total Mw of 36kDa.

      What is the source or expression system of EPOETIN Protein?
      HEK.

      What is the Purity of EPOETIN Protein?
      EPOETIN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of EPOETIN Protein?
      The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) and is typically 0.5-2.5ng/ml, corresponding to a specific activity of 400,000-2,000,000 units/mg.

      What applications can EPOETIN Protein be used in?
      EPOETIN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EPOETIN Protein?
      The endotoxin level is minimal, EPOETIN Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Epo A Human Hek
  • View Data Sheet

    Description:

    Neutrophil Activating Protein-2 (CXCL7) Human Recombinant, 95 a.a.

    Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    Product # :

    CHM-277

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    Description

    NAP 2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (35-128) and having a molecular mass of 10.3 kDa.The NAP 2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAP 2 protein 1mg/ml is supplied in 20mM Tris-HCL, pH-7.5, 1mM DTT and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.

    • Synonyms

      Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    • Physical Appearance

      NAP 2 is supplied as a sterile filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD

    • Background

      What is the molecular weight/Mw of CXCL7 95 A.A HUMAN Protein?
      CXCL7 95 A.A HUMAN Protein has a total Mw of 10.3kDa.

      What is the source or expression system of CXCL7 95 A.A HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL7 95 A.A HUMAN Protein?
      CXCL7 95 A.A HUMAN Protein is > 90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL7 95 A.A HUMAN Protein?
      The biological functionality of CXCL7 95 A.A HUMAN Protein will be determined in the future.

      What is the amino acid sequence of CXCL7 95 A.A HUMAN Protein?
      MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD

      What applications can CXCL7 95 A.A HUMAN Protein be used in?
      CXCL7 95 A.A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL7 95 A.A HUMAN Protein?
      The endotoxin level is minimal, CXCL7 95 A.A HUMAN Protein was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Nap 2 95 Aa Human
  • View Data Sheet

    Description:

    Hepatocyte Growth Factor Human Recombinant, CHO

    Scatter Factor (SF), Hepatopoietin (HPTA), HGF.

    Product # :

    CYT-251

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    Description

    Hepatocyte Growth Factor Human Recombinant produced in CHO is a heterodimer, non-glycosylated, polypeptide chain consisting an a-chain of 463 amino acids and b-chain of 234 having a total molecular mass of approximately 75kDa. The HGF is purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovarian Cells.

    Formulation

    The protein was lyophilized from a concentrated (1.4mg/ml) solution containing Phosphate-Buffered Saline with 0.02% Tween 80, pH 7.4.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of monkey 4MBr-5 indicator cells was found to be 20-40 ng/ml.

    More Info

    • Introduction

      Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.

    • Synonyms

      Scatter Factor (SF), Hepatopoietin (HPTA), HGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Hepatocyte Growth Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Hepatocyte Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      Agrees with the sequence of native human HGF.

    • Background

      What is the molecular weight/Mw of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
      HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein has a total Mw of 75kDa.

      What is the source or expression system of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
      Chinese Hamster Ovarian Cells.

      What is the Purity of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
      HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
      The ED50, calculated by the dose-dependant proliferation of monkey 4MBr-5 indicator cells was found to be 20-40 ng/ml.

      What is the amino acid sequence of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
      Agrees with the sequence of native human HGF.

      What applications can HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein be used in?
      HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
      The endotoxin level is minimal, HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Hgf Human Cho